Comparative phytochemical and biological evaluation of Egyptian Swinglea glutinosa stems and leaves
Abstract The hydroalcoholic extracts of both stems and leaves of Egyptian Swinglea glutinosa have been evaluated for their biological activities and phytochemical profiling. LC–MS/MS assists in identifying 80 phytoconstituent compounds that alternate between the stem and leaves, the majority of whic...
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| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2025-06-01
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| Series: | Scientific Reports |
| Subjects: | |
| Online Access: | https://doi.org/10.1038/s41598-025-00427-2 |
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| Summary: | Abstract The hydroalcoholic extracts of both stems and leaves of Egyptian Swinglea glutinosa have been evaluated for their biological activities and phytochemical profiling. LC–MS/MS assists in identifying 80 phytoconstituent compounds that alternate between the stem and leaves, the majority of which are new to the genus. Biological investigation results revealed the superiority of stem extract in inhibiting α-amylase and α-glucosidase enzymes scoring IC50 (15.32 ± 0.76) and (0.656 ± 0.03) over the leaves extract, which gives IC50 (112.1 ± 5.55) and (2.721 ± 0.13) respectively at (P < 0.05) and when compared to the antidiabetic standard acarbose it shows better result than it in inhibiting α-amylase and to close to it in inhibiting α-glucosidase enzymes which later score IC50 (27.2 ± 1.35)and (0.375 ± 0.02) at (P < 0.05). Stem extract also shows good inhibitory activity on acetylcholinesterase enzymes compared to standard donepezil, and that was supported by results of intermolecular docking for six compounds (2-Deoxy-2,3-dehydro-N-acetyl-neuraminic acid (DANA), ascorbic acid, glucuronic acid, protocatechuic acid, galacturonic acid, gallic acid) which only identified in stem extract. All of them show high fitting scores and strong binding interactions. Moreover, among tested compounds, DANA, ascorbic acid, and glucuronic acid have the highest-ranking scores against all target enzymes. Highly fitting and binding scores by DANA were remarkably noticed, and the molecular dynamic simulation study proved the effect of DANA against the α-amylase enzyme via decreasing the fluctuations of the enzyme’s amino acid residues due to the stabilization of enzyme-ligand complex. |
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| ISSN: | 2045-2322 |